Should you encounter any unexpected behaviour,
please let us know.

* *

CA strain for 22122720105119216

--- normal mode 7 ---

This graph displays the distance variation between successive pairs of CA atoms in the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Large distance variations can be an indicator for residue pairs that support the important strain in that particular normal mode movement. Note that residue pairs between chain breaks or at flexible ends of the protein may also exhibit large CA-CA distance variations. If more than one residues ae grouped together into a rigid block (NRBL>1), CA-CA distance variations between CA atoms in the same block will be very low.

This feature is still experimental and will be further developped in the future.

CA i CA i+1 vari
MET 1 GLU 2 0.0000

GLU 2 LEU 3 0.0130

LEU 3 ARG 4 0.0000

ARG 4 HIS 5 -0.0077

HIS 5 THR 6 -0.0001

THR 6 PRO 7 -0.0152

PRO 7 ALA 8 -0.0002

ALA 8 ARG 9 -0.0015

ARG 9 ASP 10 0.0002

ASP 10 LEU 11 -0.0019

LEU 11 ASP 12 -0.0003

ASP 12 LYS 13 -0.0235

LYS 13 PHE 14 0.0001

PHE 14 ILE 15 0.0150

ILE 15 GLU 16 0.0001

GLU 16 ASP 17 -0.0010

ASP 17 HIS 18 0.0002

HIS 18 LEU 19 0.0008

LEU 19 LEU 20 -0.0002

LEU 20 PRO 21 0.0929

PRO 21 ASN 22 0.0002

ASN 22 THR 23 0.0641

THR 23 CYS 24 0.0000

CYS 24 PHE 25 -0.0353

PHE 25 ARG 26 -0.0000

ARG 26 THR 27 -0.0005

THR 27 GLN 28 0.0000

GLN 28 VAL 29 0.0088

VAL 29 LYS 30 0.0001

LYS 30 GLU 31 0.0369

GLU 31 ALA 32 -0.0001

ALA 32 ILE 33 0.0209

ILE 33 ASP 34 -0.0002

ASP 34 ILE 35 0.0359

ILE 35 VAL 36 0.0001

VAL 36 CYS 37 0.0140

CYS 37 ARG 38 0.0001

ARG 38 PHE 39 0.0122

PHE 39 LEU 40 -0.0000

LEU 40 LYS 41 -0.0078

LYS 41 GLU 42 0.0002

GLU 42 ARG 43 0.0413

ARG 43 CYS 44 0.0001

CYS 44 PHE 45 -0.0040

PHE 45 GLN 46 0.0002

GLN 46 GLY 47 0.0051

GLY 47 THR 48 -0.0001

THR 48 ALA 49 -0.0180

ALA 49 ASP 50 0.0002

ASP 50 PRO 51 0.0370

PRO 51 VAL 52 0.0003

VAL 52 ARG 53 0.0135

ARG 53 VAL 54 -0.0001

VAL 54 SER 55 0.1584

SER 55 LYS 56 -0.0002

LYS 56 VAL 57 -0.0101

VAL 57 VAL 58 -0.0001

VAL 58 LYS 59 -0.0493

LYS 59 GLY 60 -0.0003

GLY 60 GLY 61 -0.0246

GLY 61 SER 62 -0.0003

SER 62 SER 63 -0.0420

SER 63 GLY 64 -0.0002

GLY 64 LYS 65 0.0389

LYS 65 GLY 66 -0.0001

GLY 66 THR 67 -0.0496

THR 67 THR 68 0.0001

THR 68 LEU 69 0.0064

LEU 69 ARG 70 -0.0001

ARG 70 GLY 71 0.0045

GLY 71 ARG 72 -0.0001

ARG 72 SER 73 -0.0103

SER 73 ASP 74 -0.0004

ASP 74 ALA 75 -0.0801

ALA 75 ASP 76 0.0000

ASP 76 LEU 77 -0.0374

LEU 77 VAL 78 0.0000

VAL 78 VAL 79 -0.0307

VAL 79 PHE 80 -0.0003

PHE 80 LEU 81 0.0243

LEU 81 THR 82 0.0002

THR 82 LYS 83 -0.0096

LYS 83 LEU 84 -0.0001

LEU 84 THR 85 0.0198

THR 85 SER 86 0.0001

SER 86 PHE 87 -0.0033

PHE 87 GLU 88 0.0003

GLU 88 ASP 89 -0.0298

ASP 89 GLN 90 0.0000

GLN 90 LEU 91 -0.0029

LEU 91 ARG 92 -0.0001

ARG 92 ARG 93 -0.0512

ARG 93 ARG 94 0.0001

ARG 94 GLY 95 -0.0078

GLY 95 GLU 96 -0.0004

GLU 96 PHE 97 0.0013

PHE 97 ILE 98 -0.0001

ILE 98 GLN 99 -0.0156

GLN 99 GLU 100 0.0001

GLU 100 ILE 101 0.0062

ILE 101 ARG 102 -0.0003

ARG 102 ARG 103 0.0173

ARG 103 GLN 104 -0.0003

GLN 104 LEU 105 -0.0120

LEU 105 GLU 106 0.0003

GLU 106 ALA 107 -0.0037

ALA 107 CYS 108 0.0002

CYS 108 GLN 109 0.0085

GLN 109 ARG 110 0.0002

ARG 110 GLU 111 -0.0107

GLU 111 GLN 112 0.0002

GLN 112 LYS 113 0.0133

LYS 113 PHE 114 -0.0000

PHE 114 LYS 115 0.0006

LYS 115 VAL 116 0.0001

VAL 116 THR 117 0.0186

THR 117 PHE 118 0.0001

PHE 118 GLU 119 0.0253

GLU 119 VAL 120 -0.0002

VAL 120 GLN 121 0.0277

GLN 121 SER 122 -0.0003

SER 122 PRO 123 0.0157

PRO 123 ARG 124 0.0000

ARG 124 ARG 125 -0.0287

ARG 125 GLU 126 0.0002

GLU 126 ASN 127 0.0355

ASN 127 PRO 128 -0.0001

PRO 128 ARG 129 -0.0183

ARG 129 ALA 130 -0.0001

ALA 130 LEU 131 -0.0508

LEU 131 SER 132 0.0001

SER 132 PHE 133 0.0418

PHE 133 VAL 134 0.0000

VAL 134 LEU 135 0.0168

LEU 135 SER 136 0.0001

SER 136 SER 137 0.0095

SER 137 PRO 138 -0.0003

PRO 138 GLN 139 0.0102

GLN 139 LEU 140 0.0003

LEU 140 GLN 141 -0.0153

GLN 141 GLN 142 -0.0000

GLN 142 GLU 143 0.0704

GLU 143 VAL 144 0.0001

VAL 144 GLU 145 0.0782

GLU 145 PHE 146 -0.0003

PHE 146 ASP 147 0.0403

ASP 147 VAL 148 0.0001

VAL 148 LEU 149 -0.0042

LEU 149 PRO 150 0.0002

PRO 150 ALA 151 0.0137

ALA 151 PHE 152 -0.0001

PHE 152 ASP 153 0.0225

ASP 153 ALA 154 -0.0001

ALA 154 LEU 155 0.0177

LEU 155 GLY 156 0.0001

GLY 156 GLN 157 0.0089

GLN 157 TRP 158 -0.0000

TRP 158 THR 159 0.0217

THR 159 PRO 160 -0.0002

PRO 160 GLY 161 -0.0133

GLY 161 TYR 162 -0.0003

TYR 162 LYS 163 0.0054

LYS 163 PRO 164 -0.0001

PRO 164 ASN 165 -0.0267

ASN 165 PRO 166 0.0002

PRO 166 GLU 167 0.0038

GLU 167 ILE 168 -0.0002

ILE 168 TYR 169 0.0105

TYR 169 VAL 170 -0.0001

VAL 170 GLN 171 0.0643

GLN 171 LEU 172 -0.0003

LEU 172 ILE 173 0.0144

ILE 173 LYS 174 -0.0002

LYS 174 GLU 175 -0.0011

GLU 175 CYS 176 0.0001

CYS 176 LYS 177 0.0105

LYS 177 SER 178 -0.0001

SER 178 ARG 179 -0.0041

ARG 179 GLY 180 0.0003

GLY 180 LYS 181 0.0253

LYS 181 GLU 182 0.0001

GLU 182 GLY 183 0.0260

GLY 183 GLU 184 0.0000

GLU 184 PHE 185 0.0357

PHE 185 SER 186 0.0000

SER 186 THR 187 -0.0741

THR 187 CYS 188 0.0003

CYS 188 PHE 189 0.0136

PHE 189 THR 190 0.0005

THR 190 GLU 191 -0.0385

GLU 191 LEU 192 -0.0001

LEU 192 GLN 193 -0.0306

GLN 193 ARG 194 0.0003

ARG 194 ARG 194 -0.0000

ARG 194 ASP 195 -0.0167

ASP 195 PHE 196 -0.0000

PHE 196 LEU 197 -0.0263

LEU 197 ARG 198 -0.0001

ARG 198 ASN 199 0.0472

ASN 199 ARG 200 -0.0002

ARG 200 PRO 201 0.0386

PRO 201 THR 202 -0.0001

THR 202 LYS 203 0.0401

LYS 203 LEU 204 0.0001

LEU 204 LYS 205 0.0172

LYS 205 SER 206 -0.0002

SER 206 LEU 207 0.0133

LEU 207 ILE 208 -0.0001

ILE 208 ARG 209 0.0025

ARG 209 LEU 210 -0.0001

LEU 210 VAL 211 0.0263

VAL 211 LYS 212 -0.0004

LYS 212 HIS 213 0.0131

HIS 213 TRP 214 0.0002

TRP 214 TYR 215 0.0237

TYR 215 GLN 216 0.0001

GLN 216 THR 217 -0.0162

THR 217 CYS 218 0.0001

CYS 218 LYS 219 -0.0012

LYS 219 LYS 220 -0.0000

LYS 220 THR 221 -0.0003

THR 221 HIS 222 0.0003

HIS 222 GLY 223 -0.0225

GLY 223 ASN 224 0.0002

ASN 224 LYS 225 0.0294

LYS 225 LEU 226 -0.0001

LEU 226 PRO 227 -0.0111

PRO 227 PRO 228 -0.0000

PRO 228 GLN 229 0.0437

GLN 229 TYR 230 -0.0001

TYR 230 ALA 231 -0.0176

ALA 231 LEU 232 0.0004

LEU 232 GLU 233 -0.0252

GLU 233 LEU 234 0.0002

LEU 234 LEU 235 -0.0111

LEU 235 THR 236 0.0000

THR 236 VAL 237 0.0271

VAL 237 TYR 238 0.0004

TYR 238 ALA 239 0.0186

ALA 239 TRP 240 0.0000

TRP 240 GLU 241 -0.0091

GLU 241 GLN 242 -0.0001

GLN 242 GLY 243 0.0034

GLY 243 SER 244 -0.0001

SER 244 ARG 245 0.0237

ARG 245 LYS 246 -0.0000

LYS 246 THR 247 -0.0063

THR 247 ASP 248 0.0003

ASP 248 PHE 249 0.0324

PHE 249 SER 250 0.0000

SER 250 THR 251 -0.0218

THR 251 ALA 252 0.0002

ALA 252 GLN 253 -0.0137

GLN 253 GLY 254 0.0000

GLY 254 PHE 255 0.0075

PHE 255 GLN 256 -0.0001

GLN 256 THR 257 0.0056

THR 257 VAL 258 0.0003

VAL 258 LEU 259 0.0218

LEU 259 GLU 260 0.0003

GLU 260 LEU 261 -0.0007

LEU 261 VAL 262 0.0001

VAL 262 LEU 263 0.0006

LEU 263 LYS 264 0.0004

LYS 264 HIS 265 -0.0164

HIS 265 GLN 266 0.0000

GLN 266 LYS 267 0.0381

LYS 267 LEU 268 0.0001

LEU 268 CYS 269 0.0663

CYS 269 ILE 270 0.0000

ILE 270 PHE 271 0.1035

PHE 271 TRP 272 -0.0001

TRP 272 GLU 273 0.0547

GLU 273 ALA 274 0.0001

ALA 274 TYR 275 0.0348

TYR 275 TYR 276 0.0002

TYR 276 ASP 277 -0.0052

ASP 277 PHE 278 -0.0003

PHE 278 THR 279 0.0337

THR 279 ASN 280 0.0001

ASN 280 PRO 281 0.0008

PRO 281 VAL 282 -0.0002

VAL 282 VAL 283 -0.0091

VAL 283 GLY 284 0.0000

GLY 284 ARG 285 -0.0159

ARG 285 CYS 286 0.0001

CYS 286 MET 287 -0.0165

MET 287 LEU 288 -0.0002

LEU 288 GLN 289 -0.0168

GLN 289 GLN 290 0.0000

GLN 290 LEU 291 -0.0766

LEU 291 LYS 292 0.0003

LYS 292 LYS 293 0.0656

LYS 293 PRO 294 -0.0003

PRO 294 ARG 295 -0.0232

ARG 295 PRO 296 0.0001

PRO 296 VAL 297 0.0090

VAL 297 ILE 298 -0.0001

ILE 298 LEU 299 -0.0035

LEU 299 ASP 300 0.0000

ASP 300 PRO 301 0.0020

PRO 301 ALA 302 -0.0004

ALA 302 ASP 303 0.0175

ASP 303 PRO 304 -0.0000

PRO 304 THR 305 -0.0196

THR 305 GLY 306 -0.0001

GLY 306 ASN 307 -0.1398

ASN 307 VAL 308 -0.0002

VAL 308 GLY 309 -0.0666

GLY 309 GLY 310 0.0001

GLY 310 GLY 311 0.0503

GLY 311 ASP 312 0.0002

ASP 312 THR 313 -0.0171

THR 313 HIS 314 0.0003

HIS 314 SER 315 -0.0131

SER 315 TRP 316 0.0001

TRP 316 GLN 317 -0.0074

GLN 317 ARG 318 -0.0001

ARG 318 LEU 319 -0.0024

LEU 319 ALA 320 -0.0001

ALA 320 GLN 321 0.0020

GLN 321 GLU 322 0.0001

GLU 322 ALA 323 0.0094

ALA 323 ARG 324 0.0001

ARG 324 VAL 325 -0.0025

VAL 325 TRP 326 0.0002

TRP 326 LEU 327 -0.0088

LEU 327 GLY 328 0.0002

GLY 328 TYR 329 0.0027

TYR 329 PRO 330 -0.0002

PRO 330 CYS 331 -0.0016

CYS 331 CYS 332 -0.0004

CYS 332 LYS 333 -0.0003

LYS 333 ASN 334 0.0000

ASN 334 LEU 335 0.0067

LEU 335 ASP 336 0.0001

ASP 336 GLY 337 -0.0223

GLY 337 SER 338 -0.0003

SER 338 LEU 339 -0.0005

LEU 339 VAL 340 0.0000

VAL 340 GLY 341 -0.0001

GLY 341 ALA 342 0.0000

ALA 342 TRP 343 0.0237

TRP 343 THR 344 0.0000

THR 344 MET 345 -0.0084

MET 345 LEU 346 -0.0004

LEU 346 GLN 347 0.0026

GLN 347 LYS 348 -0.0003

LYS 348 ILE 349 -0.0003

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.

Should you encounter any unexpected behaviour, please let us know.

*** ***

CA strain for 22122720105119216

--- normal mode 7 ---

Should you encounter any unexpected behaviour,
please let us know.

* *